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Protein

Catalase

Gene

katA

Organism
Proteus mirabilis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei541
Active sitei1271
Metal bindingi337Iron (heme axial ligand)1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.11.1.6. 5044.
SABIO-RKP42321.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:katA
OrganismiProteus mirabilis
Taxonomic identifieri584 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaeProteus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000849921 – 484CatalaseAdd BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53Methionine sulfone1 Publication1

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi529507.PMI1740.

Structurei

Secondary structure

1484
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 19Combined sources3
Beta strandi22 – 24Combined sources3
Helixi34 – 43Combined sources10
Beta strandi52 – 54Combined sources3
Beta strandi56 – 66Combined sources11
Turni71 – 73Combined sources3
Helixi77 – 79Combined sources3
Beta strandi85 – 93Combined sources9
Beta strandi95 – 97Combined sources3
Beta strandi103 – 107Combined sources5
Beta strandi110 – 117Combined sources8
Beta strandi120 – 130Combined sources11
Helixi137 – 139Combined sources3
Helixi140 – 147Combined sources8
Turni151 – 153Combined sources3
Helixi158 – 166Combined sources9
Helixi169 – 171Combined sources3
Helixi172 – 179Combined sources8
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Helixi188 – 190Combined sources3
Beta strandi199 – 202Combined sources4
Beta strandi208 – 217Combined sources10
Helixi226 – 235Combined sources10
Helixi239 – 249Combined sources11
Beta strandi255 – 264Combined sources10
Helixi265 – 269Combined sources5
Beta strandi271 – 273Combined sources3
Turni284 – 286Combined sources3
Beta strandi290 – 299Combined sources10
Helixi304 – 307Combined sources4
Turni308 – 310Combined sources3
Helixi328 – 345Combined sources18
Helixi349 – 351Combined sources3
Turni353 – 355Combined sources3
Beta strandi358 – 360Combined sources3
Beta strandi382 – 384Combined sources3
Beta strandi386 – 388Combined sources3
Helixi394 – 396Combined sources3
Helixi412 – 414Combined sources3
Helixi420 – 428Combined sources9
Helixi431 – 445Combined sources15
Helixi450 – 463Combined sources14
Helixi465 – 478Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E93X-ray2.00A1-484[»]
1H6NX-ray2.11A1-484[»]
1H7KX-ray2.40A2-484[»]
1M85X-ray2.00A1-484[»]
1MQFX-ray2.50A1-484[»]
1NM0X-ray2.30A1-484[»]
2CAGX-ray2.70A1-484[»]
2CAHX-ray2.70A1-484[»]
3HB6X-ray2.30A1-484[»]
ProteinModelPortaliP42321.
SMRiP42321.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42321.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42321-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE
60 70 80 90 100
RRMHAKGSGA FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG
110 120 130 140 150
AADAERDIRG FALKFYTEEG NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD
160 170 180 190 200
PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS DRGLPLSYRF VHGFGSHTYS
210 220 230 240 250
FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS QRDLFEAIER
260 270 280 290 300
GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN
310 320 330 340 350
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH
360 370 380 390 400
QIPVNAPKCP FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP
410 420 430 440 450
LSIEGAADHW NHREDEDYFS QPRALYELLS DDEHQRMFAR IAGELSQASK
460 470 480
ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG KDAK
Length:484
Mass (Da):55,614
Last modified:November 1, 1995 - v1
Checksum:iADC25F3CB41F5C50
GO

Mass spectrometryi

Molecular mass is 55643±5 Da from positions 1 - 484. Determined by ESI. 1 Publication

Sequence databases

PIRiA58663.
RefSeqiWP_004248382.1. NZ_LWUM01000109.1.

Genome annotation databases

GeneIDi6802690.

Cross-referencesi

Sequence databases

PIRiA58663.
RefSeqiWP_004248382.1. NZ_LWUM01000109.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E93X-ray2.00A1-484[»]
1H6NX-ray2.11A1-484[»]
1H7KX-ray2.40A2-484[»]
1M85X-ray2.00A1-484[»]
1MQFX-ray2.50A1-484[»]
1NM0X-ray2.30A1-484[»]
2CAGX-ray2.70A1-484[»]
2CAHX-ray2.70A1-484[»]
3HB6X-ray2.30A1-484[»]
ProteinModelPortaliP42321.
SMRiP42321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi529507.PMI1740.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6802690.

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.

Enzyme and pathway databases

BRENDAi1.11.1.6. 5044.
SABIO-RKP42321.

Miscellaneous databases

EvolutionaryTraceiP42321.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATA_PROMI
AccessioniPrimary (citable) accession number: P42321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.